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Peptide Hydrogenation and Labeling with Parahydrogen

Authors


  • We acknowledge the New York Structural Biology Center (NYSBC) for providing access to the high magnetic field facilities. We are grateful to Dr. Roman Fleysher for building the parahydrogen enrichment apparatus as part of a collaboration with Dr. Daniel K. Sodickson (Ref. 7). We would like to thank Pei Che Soon for experimental assistance during the revision. This work was supported by NSF grant CHE-0848234 (J.C.) and NSF grant CHE-0957586 (A.J.). X.X. is grateful for the Margaret and Herman Sokol fellowship. The experiments were performed in the Shared Instrument Facility of the Department of Chemistry, New York University, supported by the US National Science Foundation under Grant No. CHE0116222.

Abstract

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Site-specific spin polarization labeling of a peptide was conducted by homogeneous hydrogenation with parahydrogen. Surprisingly, polarization transfer to a remote alanine residue was observed. The diastereoselectivity of the hydrogenation reaction was determined, and these results show that parahydrogen can be used to enhance signals and elucidate the hydrogenation processes of dehydropeptide units in complex molecules.

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